Information on EC 5.3.1.8 - mannose-6-phosphate isomerase

Salmonella enterica subsp. enterica serovar Typhimurium

strain DJ77, gene pmi

Sphingobium chungbukense DJ77

strain DJ77, gene pmi

2624, 2817, 2828

biunctional phosphoglucose/phosphomannose isomerase EC 5.3.1.9 and 5.3.1.8, resp.

Swissprot

Trigonella foenum-graecum

Vigna angularis

693863

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malfunction

metabolism

physiological function

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alpha-D-fructose 6-phosphate

alpha-D-mannose 6-phosphate

Pyrococcus furiosus

694521

beta-D-mannose 6-phosphate

beta-D-fructose 6-phosphate

D-Allose

D-Psicose

D-Fructose 6-phosphate

D-fructose 6-phosphate

D-glucose 6-phosphate

D-fructose 6-phosphate

D-mannose 6-phosphate

8 entries

D-glucose 6-phosphate

D-fructose 6-phosphate

D-Lyxose

D-Xylulose

D-Mannose

D-Fructose

D-Mannose 6-phosphate

D-Mannose 6-phosphate

D-Fructose 6-phosphate

77 entries

D-Ribose

D-Ribulose

D-ribose 5-phosphate

D-ribulose 5-phosphate

D-talose

D-tagatose

L-allose

L-psicose

L-Lyxose

L-Xylulose

L-Mannose

L-Fructose

L-ribose

L-ribulose

L-ribulose

L-ribose

L-talose

L-tagatose

additional information

16 entries

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D-Fructose 6-phosphate

D-fructose 6-phosphate

D-mannose 6-phosphate

Leishmania mexicana

Q9GRS9

first step in the biosynthesis of activated mannose donors required for the biosynthesis of various glycoconjugates

652215

D-Mannose 6-phosphate

D-Mannose 6-phosphate

D-Fructose 6-phosphate

15 entries

additional information

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Ba2+

activates

Ca2+

Co2+

Cu2+

Fe2+

Mg2+

Mn2+

Ni2+

Zinc

Zn2+

additional information

9 entries

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1,10-phenanthroline

2,2'-dipyridyl

2,3-Butanedione

inactivation

5-deoxy-5-(dihydrogenophosphonomethyl)-D-arabinono-1,4-lactone

5-deoxy-5-malonyl-D-arabinonohydroxamic acid

5-deoxy-5-phosphonomethyl-D-arabinonate

5-deoxy-5-phosphonomethyl-D-arabinonohydrazide

5-deoxy-5-phosphonomethyl-D-arabinonohydroxamic acid

5-phospho-D-arabinonhydrazide

5-phospho-D-arabinonohydroxamic acid

5-phosphoarabinonate

662267

6-deoxy-6-carboxymethyl-D-mannose

6-deoxy-6-dicarboxymethyl-D-mannose

6-deoxy-6-dimethylmalonate-D-mannopyranose

6-deoxy-6-phosphonomethyl-D-mannose

6-phospho-2-deoxygluconate

Cassia coluteoides

competitive

6-phosphogluconate

6-Phosphomannonate

Cassia coluteoides

competitive

8-hydroxyquinoline

2806

ADP-glucose

0.5 mM, 77.8% of initial activity

Ag+

irreversible inhibition in a two-step process, mannose 6-phosphate protects against inactivation. Mutant enzyme Cys150Ala shows 1000fold less sensitivity than the wild-type enzyme

2818

alpha-D-mannose 6-phosphate

poor

2807

arabinose 5-phosphate

Ba2+

about 30% inhibition at 0.5 mM

benzyl 2,3,4-tri-O-benzyl-6-deoxy-6-dimethylmalonate-alpha-D-mannopyranoside

benzyl 2,3,4-tri-O-benzyl-6-O-trifluoromethanesulfonyl-alpha-D-mannose

benzyl 2,3,4-tri-O-benzyl-alpha-D-mannose

Cd2+

cysteine

2806

D-mannose 1-phosphate

0.5 mM, 81.9% of initial activity

diethyldicarbonate

dithiothreitol

EDTA

14 entries

erythrose 4-phosphate

10 entries

Fe2+

12% residual activity at 0.5 mM

fructose 1-phosphate

competitive

2821

Galactose 6-hosphate

competitive

GDP-D-mannose

inhibits mannose 6-phosphate isomerase activity of PMI, feedback regulation of this pathway

GDP-mannose

0.5 mM, 46.7% of initial activity

glucosamine 6-phosphate

competitive

glucose 1-phosphate

competitive

glucose 6-phosphate

competitive

Hg2+

HgCl2

L-ascorbic acid

Arabidopsis thaliana

1 mM, 77% residual activity

693149

mannitol 1-phosphate

N,2,3,4,5-pentahydroxypentanamide

p-chloromercuribenzoate

Arabidopsis thaliana

0.05 mM, 33% residual activity; 0.05 mM, 39% residual activity

693149

PCMB

phosphate

competitive

ribose 5-phosphate

competitive

S-nitroso-acetyl-penicillamine

dose- and time-dependent inactivation

652637

Silver sulfadiazine

sorbitol 6-phosphate

competitive

Salmonella enterica subsp. enterica serovar Typhimurium

Y3+

Zn2+

additional information

8 entries

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Ca2+

order of activation Mg2+ > Ca2+ > Mn2+ > Co2+ > Ni2+

Co2+

order of activation Mg2+ > Ca2+ > Mn2+ > Co2+ > Ni2+

diphosphate

0.5 mM, 120% of initial activity

Mg2+

order of activation Mg2+ > Ca2+ > Mn2+ > Co2+ > Ni2+

Mn2+

Mg2+ > Ca2+ > Mn2+ > Co2+ > Ni2+

Ni2+

order of activation Mg2+ > Ca2+ > Mn2+ > Co2+ > Ni2+

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0.00043 - 0.33

beta-D-mannose 6-phosphate

0.06 - 0.44

D-fructose 6-phosphate

0.72 - 3.5

D-glucose 6-phosphate

433

D-Lyxose

pH 7.5, 40°C, recombinant enzyme

946

D-mannose

pH 7.5, 40°C, recombinant enzyme

0.0413 - 243

D-mannose 6-phosphate

30 entries

110

D-ribose

pH 7.5, 40°C, recombinant enzyme

469

D-talose

pH 7.5, 40°C, recombinant enzyme

312

L-allose

pH 7.5, 40°C, recombinant enzyme

998

L-ribose

pH 7.5, 40°C, recombinant enzyme

136 - 308

L-ribulose

0.17 - 4

mannose 6-phosphate

15 entries

additional information

enzyme kinetics with D-lyxose and L-ribose, overview

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3 - 23

beta-D-mannose 6-phosphate

141

D-fructose 6-phosphate

wild type enzyme, pH 7.0, 80°C

7089

D-Lyxose

pH 7.5, 40°C, recombinant enzyme

3748

D-mannose

pH 7.5, 40°C, recombinant enzyme

0.076 - 112100

D-mannose 6-phosphate

23 entries

D-ribose

pH 7.5, 40°C, recombinant enzyme

63970

D-talose

pH 7.5, 40°C, recombinant enzyme

920

L-allose

pH 7.5, 40°C, recombinant enzyme

17600

L-ribose

pH 7.5, 40°C, recombinant enzyme

32670 - 81060

L-ribulose

121 - 162

mannose 6-phosphate

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70 - 840

beta-D-mannose 6-phosphate

641

D-fructose 6-phosphate

wild type enzyme, pH 7.0, 80°C

16.4

D-Lyxose

pH 7.5, 40°C, recombinant enzyme

3.5

D-mannose

pH 7.5, 40°C, recombinant enzyme

13 - 6685

D-mannose 6-phosphate

12 entries

0.6

D-ribose

pH 7.5, 40°C, recombinant enzyme

6.8

D-talose

pH 7.5, 40°C, recombinant enzyme

2.9

L-allose

pH 7.5, 40°C, recombinant enzyme

17.6

L-ribose

pH 7.5, 40°C, recombinant enzyme

182 - 579

L-ribulose

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0.162

5-deoxy-5-malonyl-D-arabinonohydroxamic acid

in 50 mM HEPES buffer, pH 7.1, at 25°C

0.0006 - 0.002

5-phospho-D-arabinonhydrazide

0.000041 - 0.0008

5-phospho-D-arabinonohydroxamic acid

0.0105 - 0.115

6-deoxy-6-dicarboxymethyl-D-mannose

0.11 - 58

6-phosphogluconate

0.035 - 0.164

erythrose 4-phosphate

0.0014

erythrose-4-phosphate

pH 7.4, 50°C

N,2,3,4,5-pentahydroxypentanamide

in 50 mM HEPES buffer, pH 7.1, at 25°C

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5-deoxy-5-phosphonomethyl-D-arabinonate

Escherichia coli

above, pH 7.1, 25°C, recombinant enzyme

702663

5-deoxy-5-phosphonomethyl-D-arabinonohydrazide

Escherichia coli

above, pH 7.1, 25°C, recombinant enzyme

702663

0.37 - 2.2

5-deoxy-5-phosphonomethyl-D-arabinonohydroxamic acid

0.9 - 4.6

6-deoxy-6-carboxymethyl-D-mannose

0.0181 - 0.199

6-deoxy-6-dicarboxymethyl-D-mannose

1.61 - 4.7

6-deoxy-6-phosphonomethyl-D-mannose

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0.01

wild type enzyme, using ribose 5-phosphate as substrate, at pH 7.0 and 80°C

0.0101

recombinant enzyme

0.0165

recombinant enzyme

0.0225

recombinant enzyme

0.0659

recombinant enzyme

0.0918

recombinant enzyme

0.269

enzyme activity in cells after 54 h growth on maltose

701879

0.3

mutant enzyme E132D, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C; mutant enzyme W13A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C

0.306

Alcaligenes sp.

enzyme activity in cells after 54 h growth on sucrose

701879

0.313

Alcaligenes sp.

enzyme activity in cells after 54 h growth on glucose

701879

0.6

mutant enzyme E67Q, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C

0.74

wild type enzyme, using ribulose 5-phosphate as substrate, at pH 7.0 and 80°C

1.4

mutant enzyme E132A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C

1.5

mutant enzyme H122Q, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C; mutant enzyme H50Q, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C; mutant enzyme Q48A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C

1.7

mutant enzyme H50A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C

1.9

mutant enzyme E67A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C; mutant enzyme R142A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C

2.1

mutant enzyme H122A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C

2.8

mutant enzyme E67D, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C

3 - 8

mutant enzyme W69A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C

wild type enzyme, using D-psicose as substrate, at pH 7.0 and 75°C

4.5

wild type enzyme, using D-fructose 6-phosphate as substrate, at pH 7.0 and 80°C

5.95

mutant enzyme K65A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C

wild type enzyme, using L-mannose as substrate, at pH 7.0 and 75°C

wild type enzyme, using L-xylulose as substrate, at pH 7.0 and 75°C

wild type enzyme, using L-lyxose as substrate, at pH 7.0 and 75°C

mutant enzyme W13F, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C

33.5

mutant enzyme W13H, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C; mutant enzyme Y124A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C

mutant enzyme L39A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C

wild type enzyme, using L-psicose as substrate, at pH 7.0 and 75°C

mutant enzyme D138A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C

mutant enzyme W13Y, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C

wild type enzyme, using L-fructose as substrate, at pH 7.0 and 75°C

wild type enzyme, using L-talose as substrate, at pH 7.0 and 75°C

wild type enzyme, using D-tagatose as substrate, at pH 7.0 and 75°C

126

wild type enzyme, using D-ribulose as substrate, at pH 7.0 and 75°C

128

wild type enzyme, using D-xylulose as substrate, at pH 7.0 and 75°C

165

wild type enzyme, using D-allose as substrate, at pH 7.0 and 75°C

167

wild type enzyme, using D-fructose as substrate, at pH 7.0 and 75°C

194

mutant enzyme R11A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C

333

wild type enzyme, using D-lyxose as substrate, at pH 7.0 and 75°C

380

2828

420

2828

425

wild type enzyme, using L-ribose as substrate, at pH 7.0 and 75°C

474

mutant enzyme K37A, using L-ribulose as substrate, at pH 7.0 and 75°C

742

wild type enzyme, using L-allose as substrate, at pH 7.0 and 75°C

838

mutant enzyme W13A, using L-ribulose as substrate, at pH 7.0 and 75°C

842

wild type enzyme, using D-mannose as substrate, at pH 7.0 and 75°C

890

purified recombinant enzyme

972

mutant enzyme D138A, using L-ribulose as substrate, at pH 7.0 and 75°C

1011

mutant enzyme K65A, using L-ribulose as substrate, at pH 7.0 and 75°C

1016

mutant enzyme Q48A, using L-ribulose as substrate, at pH 7.0 and 75°C

1045

mutant enzyme R142E, using L-ribulose as substrate, at pH 7.0 and 75°C

1046

mutant enzyme W69A, using L-ribulose as substrate, at pH 7.0 and 75°C

1065

mutant enzyme L39A, using L-ribulose as substrate, at pH 7.0 and 75°C

1076

mutant enzyme L124A, using L-ribulose as substrate, at pH 7.0 and 75°C

1092

mutant enzyme R142Y, using L-ribulose as substrate, at pH 7.0 and 75°C

1194

mutant enzyme L18A, using L-ribulose as substrate, at pH 7.0 and 75°C

1214

mutant enzyme R142K, using L-ribulose as substrate, at pH 7.0 and 75°C

1270

mutant enzyme R142Q, using L-ribulose as substrate, at pH 7.0 and 75°C

1482

mutant enzyme R11A, using L-ribulose as substrate, at pH 7.0 and 75°C

1493

wild type enzyme, using L-ribulose as substrate, at pH 7.0 and 75°C

1619

wild type enzyme, using D-talose as substrate, at pH 7.0 and 75°C

1791

mutant enzyme R142A, using L-ribulose as substrate, at pH 7.0 and 75°C

2152

mutant enzyme R14N, using L-ribulose as substrate, at pH 7.0 and 75°C

additional information

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6.5 - 7

6.5 - 8

7 - 7.2

7.1

7.4

7.5

7.6

Salmonella enterica subsp. enterica serovar Typhimurium

8.5

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5.5 - 9

about 50% of maximal activity at pH 5.5 and pH 9.0

6 - 11

Cassia coluteoides

pH 6.0: 50% of maximal activity, relative high activity up to pH 11

6.3 - 8.8

more than 50% of maximum activity in this range

6.5 - 8.5

Salmonella enterica subsp. enterica serovar Typhimurium

6.5 - 9

activity range

6.5 - 8.5

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Salmonella enterica subsp. enterica serovar Typhimurium

assay at room temperature

recombinant enzyme

maximal activity of the recombinant enzyme for L-ribulose isomerization

Pyrococcus horikoshii

O58649

733811

100

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20 - 50

60 - 80

70 - 90

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5.9

calculated

calculated

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cell suspension culture

Vigna angularis

growth on liquid and solid media, but no in presence of 90 mM mannose. After transfer of sucrose-grown cell onto medium containing mannose, cells grew little initially, but after a month lag period, they start to form callus colonies. Mannose-accomodated cells are capable of converting mannose to sucrose, with enhanced phosphomannose isomerase activity

693863

corm

digestive gland

Placopecten magellanicus

Placopecten magellanicus

pod

Cassia coluteoides

developing and germinating

additional information

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2gz6, download, 3D-view

1qwr, download, 3D-view

SCOPe (1qwr)

CATH (1qwr)

Bacillus subtilis (strain 168)

P39841

1pmi, download, 3D-view

SCOPe (1pmi)

CATH (1pmi)

Candida albicans (strain SC5314 / ATCC MYA-2876)

P34948

1tzb, download, 3D-view

SCOPe (1tzb)

CATH (1tzb)

Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)

1tzc, download, 3D-view

SCOPe (1tzc)

CATH (1tzc)

Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)

1x9h, download, 3D-view

SCOPe (1x9h)

CATH (1x9h)

Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)

1x9i, download, 3D-view

SCOPe (1x9i)

CATH (1x9i)

Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)

2wfp, download, 3D-view

SCOPe (2wfp)

CATH (2wfp)

Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

3h1m, download, 3D-view

SCOPe (3h1m)

CATH (3h1m)

Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

3h1w, download, 3D-view

SCOPe (3h1w)

CATH (3h1w)

Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

3h1y, download, 3D-view

SCOPe (3h1y)

CATH (3h1y)

Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

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29000

29054

29100

gel filtration

33548

2 * 36000, SDS-PAGE, 2 * 33548, calculated

35000

Q9HIC2

2 * 35000, SDS-PAGE, 2 * 35150, calculated

662220

35150

Q9HIC2

2 * 35000, SDS-PAGE, 2 * 35150, calculated

36000

36100

2 * 36000, SDS-PAGE, 2 * 36100, calculated

662220

36444

* 36500, recombinant enzyme, SDS-PAGE, 1 * 36444, sequence calculation

36452

1 * 36000, recombinant enzyme, SDS-PAGE, 1 * 36452, sequence calculation

36500

* 36500, recombinant enzyme, SDS-PAGE, 1 * 36444, sequence calculation

36600

gel filtration, recombinant enzyme

45000

46520

calculation from nucleotide sequence encoded by cDNA

2826

46530

recombinant enzyme, electrospray mass spectroscopy

2826

48000

Q9HIC2

gel filtration

662220

48740

wild-type recombinant enzyme, electrospray mass spectroscopy

49060

selenomethionine-labelled enzyme expressed in E. coli, electrospray mass spectroscopy

50000

x * 50000, recombinant His6-tagged enzyme, SDS-PAGE

52900

Pyrococcus horikoshii

x * 52900, SDS-PAGE

53000

SDS-PAGE

54000

55000

x * 55300, calculated, x * 55000, SDS-PAGE

671785

55300

Burkholderia cepacia

Q06XM8

x * 55300, calculated, x * 55000, SDS-PAGE

671785

55716

x * 55716, calculated, x * 56000, SDS-PAGE

56000

58000

Trigonella foenum-graecum

gel filtration

59000

gel filtration

61000

x * 61000, calculation from nucleotide sequence

2829

63000

gel filtration

65000

sedimentation equilibrium, analytical ultracentrifugation

67000

68000

Cassia coluteoides

enzyme from pods, gel filtration

74500

Cassia coluteoides

enzyme from pods and seeds, density gradient centrifugation

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10 entries

dimer

monomer

additional information

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2820, 2822, 2825

homology modeling of structure and refinement by energy minimization and molecular dynamics

681498

660585

both in complex with fructose 6-phosphate and with glucose 6-phosphate

661100

both native form and in complex with 5-phosphoarabinonate

Salmonella enterica subsp. enterica serovar Typhimurium

662267

enzyme in apoform without metal ion, in the holoform with bound Zn2+, or complexed with bound inhibitor yttrium, or with Zn2+ and fructose 6-phosphate, microbatch method, 0.003 ml of protein solution and crystallization solution are mixed containing 4 mg/ml protein, 0.1 M magnesium acetate, 0.2 M sodium cacodylate, pH 6.5, 20% PEG 8000 and 5% dioxane, addition of 10 mM metal ions and 250 mM fructose 6-phosphate for complexed enzyme, X-ray diffraction structure determination and analysis at 1.7-2.5 A resolution, molecular replacement

Salmonella enterica subsp. enterica serovar Typhimurium

to 1.66 A resolution, space group P212121. Preliminary structure solution by molecular replacement using the strucutre from Candida albicans mannose-6-phosphate isomerase

690273

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5.5

40°C, 1 h, about 35% loss of activity

2810

6 - 9.5

40°C, 1 h, no loss of activity

2810

6.5 - 8

4°C, stable

2827

40°C, 1 h, about 25% loss of activity

2810

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purified recombinant enzyme, half-life is 461 h

half-life in absence of Zn2+: 110 min, half-life in presence of 0.0002 mM ZnCl2: 270 min

purified recombinant enzyme, half-life is 325 h

purified recombinant enzyme, half-life is 236 h

6 min, wild-type enzyme stable, mutant enzyme loses about 90% of activity

purified recombinant enzyme, half-life is 10 h

pH 6.5, 10 min, about 75% loss of native enzyme

enzyme half-life is 388 h

64 - 85

the half-lives of the enzyme at 65, 70, 75, 80, and 85°C are 13, 6.5, 3.7, 1.8, and 0.2 h, respectively

enzyme half-life is 73 h

65 - 85

the enzyme shows half-lives of 22, 10, 5.5, 2.1, and 0.3 h at 65, 70, 75, 80, and 85°C, respectively

enzyme half-life is 27 h

100

melting temperature for thermal unfolding, 60 min, 50% residual activity

additional information

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EDTA-treated enzyme and 1,10-phenanthroline-treated enzyme is more susceptible to heat denaturation, addition of various metal ions causes the recovery of thermal stability. The most effective metal ion is Co2+, which causes the recovery of thermal stability to a level higher than that of the native enzyme

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-20°C, unstable

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HisTrap HP column chromatography

HiTrap Ni-chelating column chromatography and Q-Sepharose column chromatography

Ni-affinity column

normal and selenomethionine-labelled enzyme expressed in Escherichia coli

recombinant enzyme 27fold from Escherichia coli strain ER2566 by affinity chromatography

recombinant enzyme 8.7fold from Escherichia coli strain ER2566

recombinant His6-tagged enzyme from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography

Salmonella enterica subsp. enterica serovar Typhimurium

recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography

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Agrobacterium-based expression in Linum usitatissimum

682360

cDNA under the control of the GAL1 promoter, expression in Saccharomyces cerevisiae and in Escherichia coli

2826

expressed in Escherichia coli BL21 Codon Plus (DE3)-RIPL strain

Pyrococcus furiosus

694521

expressed in Escherichia coli ER2566 cells

expressed in Escherichia coli GI724 cells

Brassica rapa subsp. chinensis

716883

expressed in Nicotiana tabacum transformed with Agrobacterium tumefaciens

G1E7A7

728283

expressed in Oryza sativa ssp. japonica varieties Wanjing97 and Nipponbare

728469

expression in Agrobacterium tumefaciens

Arabidopsis thaliana

Q9M884

700488

expression in Brassica rapa

681607, 682359

expression in Escherichia coli

expression in Escherichia coli strain ER2566

expression in Escherichia coli strain ER2566, coexpression with L-arabinose isomerase

701812

expression in Pseudomonas aeruginosa

3354

gene pmi, DNA and amino acid sequence determination and analysis, expression of the His6-tagged enzyme in Escherichia coli strain BL21 (DE3)

high level expression in Escherichia coli M15 as inclusion bodies

Leishmania mexicana

Q9GRS9

652215

overexpressed under the control of the tac promoter in the broad-host-range controlled-expression vector pMMB22, expression in Escherichia coli

2814

overexpression in both mucoid and nonmucoid strains of Pseudomonas aeruginosa

Salmonella enterica subsp. enterica serovar Typhimurium

3354

overexpression of the N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)

use of enzyme as selectable marker

682353

wild-type and selenomethionine-labelled enzyme expressed in Escherichia coli

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C150A

mutant Cys150Ala shows similar Km-values and maximal velocity as compared to the wild-type enzyme. The mutant enzyme shows no inhibition by silver sulfadiazine, and is 1000fold less sensitive to Hg2+ inhibition

2818

L129F

the activity of the mutant is 204% of the activity of the wild type enzyme

L129W

the activity of the mutant is 10% of the activity of the wild type enzyme

L129Y

the activity of the mutant is 94% of the activity of the wild type enzyme

N90A/L129F

the activity of the mutant is about 6fold higher than the activity of the wild type enzyme

W17Q/N90A/L129F

the specific activity and catalytic efficiency for L-ribulose isomerization of this variant are 3.1 and 7.1fold higher, respectively, than those of the wild type enzyme at pH 7.0 and 70°C in the presence of 1mM Co2+

E410A

about 25% of wild-type catalytic efficiency

E458A

about 25% of wild-type catalytic efficiency

H411A

about 25% of wild-type catalytic efficiency

N433A

about 25% of wild-type catalytic efficiency

R373A

about 4% of wild-type catalytic efficiency

R408A

complete loss of phosphomannose isomerase activity without affecting guanosine diphosphate-D-mannose diphosphorylase activity

R408K

complete loss of phosphomannose isomerase activity without affecting guanosine diphosphate-D-mannose diphosphorylase activity

R472A

about 1% of wild-type catalytic efficiency

R479A

about 3% of wild-type catalytic efficiency

E410A

about 25% of wild-type catalytic efficiency

H411A

about 25% of wild-type catalytic efficiency

R408A

complete loss of phosphomannose isomerase activity without affecting guanosine diphosphate-D-mannose diphosphorylase activity

R408K

complete loss of phosphomannose isomerase activity without affecting guanosine diphosphate-D-mannose diphosphorylase activity

R479A

about 3% of wild-type catalytic efficiency

D138A

E132A

E132D

the mutant shows 0.4% activity compared to the wild type enzyme

E132K

inactive

E132Q

inactive

E132W

inactive

E67A

E67D

the mutant shows 3.7% activity compared to the wild type enzyme

E67K

inactive

E67Q

the mutant shows 0.8% activity compared to the wild type enzyme

E67W

inactive

H122A

H122D

inactive

H122K

inactive

H122Q

the mutant shows 2.0% activity compared to the wild type enzyme

H122W

inactive

H50A

H50D

inactive

H50K

inactive

H50Q

the mutant shows 2.0% activity compared to the wild type enzyme

H50W

inactive

K37A

K65A

L124A

the enzyme shows decreased specific activity for L-ribulose

L18A

L39A

Q48A

Q48D

inactive

Q48K

inactive

Q48N

inactive

Q48W

inactive

R11A

R142A

R142D

inactive

R142E

the enzyme shows decreased specific activity for L-ribulose

R142K

R142N

R142Q

the enzyme shows decreased specific activity for L-ribulose

R142W

inactive

R142Y

the enzyme shows decreased specific activity for L-ribulose

W13A

W13D

inactive

W13F

the mutant shows 41% activity compared to the wild type enzyme

W13H

the mutant shows 52% activity compared to the wild type enzyme

W13K

inactive

W13Q

inactive

W13Y

the mutant shows 68% activity compared to the wild type enzyme

W69A

Y124A

the mutant shows 52% activity compared to the wild type enzyme

E132A

the mutants has no activity for L-ribulose; the mutant shows 1.9% activity compared to the wild type enzyme

E132D

the mutant shows 0.4% activity compared to the wild type enzyme

E132Q